ID   PPAD_YEAST              Reviewed;         468 AA.
AC   P52290; D6VRW7;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   04-NOV-2026, entry version 167.
DE   RecName: Full=Probable acid phosphatase DIA3;
DE            EC=3.1.3.2;
DE   AltName: Full=Digs into agar protein 3;
DE   Flags: Precursor;
GN   Name=DIA3; OrderedLocusNames=YDL024C; ORFNames=D2815;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169867; DOI=10.1038/387s075;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA   Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA   Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA   Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA   Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA   Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA   Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA   Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA   Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA   Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA   Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA   Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA   Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA   Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA   Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA   Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA   Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA   Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA   Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA   Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a phosphate monoester + H2O = an alcohol + phosphate;
CC         Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.2;
CC   -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC       {ECO:0000305}.
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DR   EMBL; Z48432; CAA88335.1; -; Genomic_DNA.
DR   EMBL; Z74072; CAA98583.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA11827.1; -; Genomic_DNA.
DR   PIR; S52495; S52495.
DR   RefSeq; NP_010260.1; NM_001180083.1.
DR   AlphaFoldDB; P52290; -.
DR   SMR; P52290; -.
DR   BioGRID; 32031; 29.
DR   DIP; DIP-5014N; -.
DR   FunCoup; P52290; 407.
DR   IntAct; P52290; 2.
DR   STRING; 4932.YDL024C; -.
DR   GlyCosmos; P52290; 11 sites, No reported glycans.
DR   GlyGen; P52290; 11 sites.
DR   PaxDb; 4932-YDL024C; -.
DR   PeptideAtlas; P52290; -.
DR   EnsemblFungi; YDL024C_mRNA; YDL024C; YDL024C.
DR   GeneID; 851537; -.
DR   KEGG; sce:YDL024C; -.
DR   AGR; SGD:S000002182; -.
DR   SGD; S000002182; DIA3.
DR   VEuPathDB; FungiDB:YDL024C; -.
DR   eggNOG; KOG1382; Eukaryota.
DR   HOGENOM; CLU_020880_3_1_1; -.
DR   InParanoid; P52290; -.
DR   OMA; AACVAPI; -.
DR   OrthoDB; 6509975at2759; -.
DR   BioCyc; YEAST:G3O-29451-MONOMER; -.
DR   BioGRID-ORCS; 851537; 1 hit in 10 CRISPR screens.
DR   PRO; PR:P52290; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; P52290; protein.
DR   GO; GO:0071944; C:cell periphery; HDA:SGD.
DR   GO; GO:0030287; C:cell wall-bounded periplasmic space; IBA:GO_Central.
DR   GO; GO:0009277; C:fungal-type cell wall; IDA:SGD.
DR   GO; GO:0003993; F:acid phosphatase activity; ISS:SGD.
DR   GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR   GO; GO:0001403; P:invasive growth in response to glucose limitation; IGI:SGD.
DR   GO; GO:0007124; P:pseudohyphal growth; IMP:SGD.
DR   CDD; cd07061; HP_HAP_like; 1.
DR   FunFam; 3.40.50.1240:FF:000021; Acid phosphatase; 1.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR   InterPro; IPR033379; Acid_Pase_AS.
DR   InterPro; IPR000560; His_Pase_clade-2.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   InterPro; IPR016274; Histidine_acid_Pase_euk.
DR   PANTHER; PTHR20963:SF18; ACID PHOSPHATASE PHO11-RELATED; 1.
DR   PANTHER; PTHR20963; MULTIPLE INOSITOL POLYPHOSPHATE PHOSPHATASE-RELATED; 1.
DR   Pfam; PF00328; His_Phos_2; 1.
DR   PIRSF; PIRSF000894; Acid_phosphatase; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR   PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
DR   PROSITE; PS00778; HIS_ACID_PHOSPHAT_2; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Hydrolase; Reference proteome; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000250"
FT   CHAIN           21..468
FT                   /note="Probable acid phosphatase DIA3"
FT                   /id="PRO_0000023958"
FT   ACT_SITE        76
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        339
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        98
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        163
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        193
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        202
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        238
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        251
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        316
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        357
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        391
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        457
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        462
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   468 AA;  53076 MW;  1F07FF374DDF162C CRC64;
     MVKPVIFAIC LGVLLSKALS IPLRSFADIE LIGSQKSLFP FLGGSAPYFS FPANYGIPTD
     IPEGCRLTQV QMIGRHGERY PTRSEAKDIF EVWYKISNYT GKYEGSLSFL NNGYEFFIPD
     ESLLEMETTL QNSIDVLNPY TGEMNAKRHA REFLAKYGKL MENCTNFPIF TTNSKRIYDT
     AQYFAEALGD GFNISLQTLS ENSSSGANTL AAKSSCPNWN SNANNDILMS YSRDYLENIS
     DRLNDENKGL NLSRKDAAAL FSWCAFELNA KGYSNICDIF SAAELIHYSY ETDLTSFYQN
     GPGYKLIKSI GANLFNATVK LIRQSAHLDQ KVWLSFTHDT DILNYLTTAG LIDDTRNLTT
     NHVPFRDHSY HRSWYIPQGA RVYTEKFQCS NDSYVRYVVN DAVVPIESCS SGPGFSCEEG
     TFYEYAKDRL RGVSFYEDCD VSKVSKEKEL TFYWDWNTTR YNASLVNQ
//